MMK1_MEDSA
ID MMK1_MEDSA Reviewed; 387 AA.
AC Q07176;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Mitogen-activated protein kinase homolog MMK1;
DE EC=2.7.11.24;
DE AltName: Full=MAP kinase ERK1;
DE AltName: Full=MAP kinase MSK7;
GN Name=MMK1; Synonyms=ERK1, MSK7;
OS Medicago sativa (Alfalfa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3879;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Embryo;
RX PubMed=8220466; DOI=10.1046/j.1365-313x.1993.03040611.x;
RA Jonak C., Pay A., Boegre L., Hirt H., Heberle-Bors E.;
RT "The plant homologue of MAP kinase is expressed in a cell cycle-dependent
RT and organ-specific manner.";
RL Plant J. 3:611-617(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PHOSPHORYLATION AT TYR-215.
RC STRAIN=cv. Iroquois; TISSUE=Seedling root;
RX PubMed=8439746; DOI=10.2307/3869431;
RA Duerr B., Gawienowski M., Ropp T., Jacobs T.;
RT "MsERK1: a mitogen-activated protein kinase from a flowering plant.";
RL Plant Cell 5:87-96(1993).
CC -!- FUNCTION: May play a role in the mitogenic induction of symbiotic root
CC nodules on Alfalfa by Rhizobium signal molecules.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.24;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.24;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC phosphorylation. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Roots and stems.
CC -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC whose phosphorylation activates the MAP kinases.
CC -!- PTM: Dually phosphorylated on Thr-213 and Tyr-215, which activates the
CC enzyme (By similarity). Autophosphorylated. {ECO:0000250,
CC ECO:0000269|PubMed:8439746}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MAP kinase subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X66469; CAA47099.1; -; mRNA.
DR EMBL; L07042; AAB41548.1; -; mRNA.
DR PIR; S48123; S48123.
DR AlphaFoldDB; Q07176; -.
DR SMR; Q07176; -.
DR iPTMnet; Q07176; -.
DR BRENDA; 2.7.11.24; 3078.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004707; F:MAP kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR003527; MAP_kinase_CS.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS01351; MAPK; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Conjugation; Kinase; Mitosis;
KW Nucleotide-binding; Phosphoprotein; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..387
FT /note="Mitogen-activated protein kinase homolog MMK1"
FT /id="PRO_0000186317"
FT DOMAIN 55..340
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOTIF 213..215
FT /note="TXY"
FT ACT_SITE 181
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 61..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 213
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 215
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:8439746"
SQ SEQUENCE 387 AA; 44402 MW; 8672871A3D34EAD2 CRC64;
MEGGGAPPAD TVMSDAAPAP PQMGIENIPA VLSHGGRFIQ YNIFGNIFEV TAKYKPPIMP
IGKGAYGIVC SAHNSETNEH VAVKKIANAF DNKIDAKRTL REIKLLRHMD HENVVAIRDI
VPPPQREVFN DVYIAYELMD TDLHQIIRSN QALSEEHCQY FLYQILRGLK YIHSANVLHR
DLKPSNLLLN ANCDLKICDF GLARVTSETD FMTEYVVTRW YRAPELLLNS SDYTAAIDVW
SVGCIFMELM DRKPLFPGRD HVHQLRLLME LIGTPSEDDL GFLNENAKRY IRQLPPYRRQ
SFQEKFPHVH PEAIDLVEKM LTFDPRKRIT VEDALAHPYL TSLHDISDEP VCMTPFSFDF
EQHALTEEQM KELIYREALA FNPEYQQ
